2021-03-232013-04-260163386415206025WOS;000355215900006SCOPUS;2-s2.0-84929657569http://hdl.handle.net/10784/26790Bacillus subtilis EA-CB0015 was isolated from the phyllosphere of a banana plant and tested for its potential to produce bioactive compounds against Mycosphaerella fijiensis. Using a dual plate culture technique the cell-free supernatant of B. subtilis EA-CB0015 produced inhibition values of 89 +/- 1%. The active compounds were purified by solid-phase extraction and HPLC, and their primary structures determined using mass spectrometry and amino acid analysis. A new fengycin isoform, fengycin C, with the amino acid sequence Glu-Orn-Tyr-Thr-Glu-Val-Pro-Gln-Thr-Ile was isolated. The peptidic moiety differs from fengycin B at position 9 and from fengycin A at positions 6 and 9. The beta-hydroxy fatty acyl chain is connected to the N-terminal of the decapeptide and can be saturated or unsaturated, ranging from 14 to 18 carbons. The C-terminal residue of the peptidic moiety is linked to the tyrosine residue at position 3, forming the branching point of the acyl peptide and the eight-membered cyclic lactone.enghttps://v2.sherpa.ac.uk/id/publication/issn/0163-3864Fengycin C produced by Bacillus subtilis EA-CB0015.articleamino acidantifungal agentfengycin cnatural producttyrosineunclassified drugarticleBacillus subtilisbacterial strainbacterium isolationbiological activitycarboxy terminal sequencecell free systemculture techniquedrug structuredrug synthesisfungushigh performance liquid chromatographymass spectrometryMycosphaerella fijiensisnonhumannucleotide sequencesolid phase extractionAmino Acid SequenceAntifungal AgentsAscomycotaBacillus subtilisLipopeptidesMicrobial Sensitivity TestsMolecular StructureMusaPeptidesCyclicProtein IsoformsTyrosineBacillus subtilisMycosphaerella fijiensis2021-03-23Villegas-Escobar, ValeskaCeballos, IsabelMira, John J.Edith Argel, LuzOrduz Peralta, SergioRomero-Tabarez, Magally10.1021/np300574v